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Observation of a tight-turn conformation in a proline-containing inhibitor of renin angiotensin

✍ Scribed by Sudha Srivastava; Ratna S. Phadke; Girjesh Govil

Publisher: John Wiley and Sons
Year: 1989
Tongue: English
Weight: 344 KB
Volume: 27
Category: Article
ISSN: 0749-1581
DOI: 10.1002/mrc.1260270507

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✦ Synopsis

The solution conformation of renin inhibitor peptide, Pro-His-Pro-Phe-His-Phe-Phe-Val-Tyr-Lys, was established using proton magnetic resonance techniques. As a first step a complete resonance assignment was made in DMSO-d6 using 2D NMR techniques. Some of the backbone N H protons show a very low temperature coefficient, indicating their involvement in intramolecular hydrogen bonding. The 3J(NH-Ca, H) values the inter-residue NOES, the temperature coefficient of the backbone NH protons and the chemical shift positions indicate the presence of a tight turn in the molecule. A model is proposed, using computer graphics, based on the experimental results.

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